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Journal Article

Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.

MPS-Authors
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Burkhardt,  P.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Fasshauer,  D.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1473674.pdf
(Publisher version), 2MB

Supplementary Material (public)

1473674_1.pdf
(Supplementary material), 2MB

Citation

Meijer, M., Burkhardt, P., de Wit, H., Toonen, R. F., Fasshauer, D., & Verhage, M. (2012). Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. The EMBO Journal, 31(9), 2156-2168. doi:10.1038/emboj.2012.72.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-9B5C-1
Abstract
Synaptic transmission depends critically on the Sec1p/Munc18 protein Munc18-1, but it is unclear whether Munc18-1 primarily operates as a integral part of the fusion machinery or has a more upstream role in fusion complex assembly. Here, we show that point mutations in Munc18-1 that interfere with binding to the free Syntaxin1a N-terminus and strongly impair binding to assembled SNARE complexes all support normal docking, priming and fusion of synaptic vesicles, and normal synaptic plasticity in munc18-1 null mutant neurons. These data support a prevailing role of Munc18-1 before/during SNARE-complex assembly, while its continued association to assembled SNARE complexes is dispensable for synaptic transmission.